PARP_SACSO
ID PARP_SACSO Reviewed; 231 AA.
AC B3EWG9;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=NAD(+) ADP-ribosyltransferase {ECO:0000303|PubMed:9761745};
DE Short=PARPSss {ECO:0000303|PubMed:9761745};
DE EC=2.4.2.30 {ECO:0000269|PubMed:9761745};
DE AltName: Full=Poly(ADP-ribose) polymerase-like thermozyme {ECO:0000303|PubMed:9761745};
DE Flags: Fragments;
OS Saccharolobus solfataricus (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=2287;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
RC STRAIN=DSM 5833 / MT-4 {ECO:0000269|PubMed:19007307};
RX PubMed=19007307; DOI=10.1515/bc.2009.006;
RA Di Maro A., De Maio A., Castellano S., Parente A., Farina B.,
RA Faraone-Mennella M.R.;
RT "The ADP-ribosylating thermozyme from Sulfolobus solfataricus is a DING
RT protein.";
RL Biol. Chem. 390:27-30(2009).
RN [2] {ECO:0000305}
RP FUNCTION.
RC STRAIN=DSM 5833 / MT-4 {ECO:0000269|PubMed:8549833};
RX PubMed=8549833; DOI=10.1016/0014-5793(95)01455-1;
RA Faraone-Mennella M.R., Gambacorta A., Nicolaus B., Farina B.;
RT "Immunochemical detection of ADP-ribosylating enzymes in the archaeon
RT Sulfolobus solfataricus.";
RL FEBS Lett. 378:199-201(1996).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DSM 5833 / MT-4 {ECO:0000269|PubMed:9761745};
RX PubMed=9761745; DOI=10.1042/bj3350441;
RA Faraone-Mennella M.R., Gambacorta A., Nicolaus B., Farina B.;
RT "Purification and biochemical characterization of a poly(ADP-ribose)
RT polymerase-like enzyme from the thermophilic archaeon Sulfolobus
RT solfataricus.";
RL Biochem. J. 335:441-447(1998).
RN [4] {ECO:0000305}
RP ACTIVITY REGULATION.
RC STRAIN=DSM 5833 / MT-4 {ECO:0000269|PubMed:11040421};
RX PubMed=11040421; DOI=10.1111/j.1574-6968.2000.tb09351.x;
RA Faraone Mennella M.R., Castellano S., De Luca P., Discenza A.,
RA Gambacorta A., Nicolaus B., Farina B.;
RT "Comparison of the ADP-ribosylating thermozyme from Sulfolobus solfataricus
RT and the mesophilic poly(ADP-ribose) polymerases.";
RL FEMS Microbiol. Lett. 192:9-14(2000).
RN [5] {ECO:0000305}
RP FUNCTION.
RC STRAIN=DSM 5833 / MT-4 {ECO:0000269|PubMed:11891858};
RX PubMed=11891858; DOI=10.1002/jcb.10107;
RA Faraone-Mennella M.R., Piccialli G., De Luca P., Castellano S.,
RA Giordano A., Rigano D., De Napoli L., Farina B.;
RT "Interaction of the ADP-ribosylating enzyme from the hyperthermophilic
RT archaeon S. solfataricus with DNA and ss-oligo deoxy ribonucleotides.";
RL J. Cell. Biochem. 85:146-157(2002).
RN [6] {ECO:0000305}
RP FUNCTION.
RC STRAIN=DSM 5833 / MT-4 {ECO:0000269|PubMed:11891859};
RX PubMed=11891859; DOI=10.1002/jcb.10108;
RA Faraone-Mennella M.R., De Luca P., Giordano A., Gambacorta A., Nicolaus B.,
RA Farina B.;
RT "High stability binding of poly(ADPribose) polymerase-like thermozyme from
RT S. solfataricus with circular DNA.";
RL J. Cell. Biochem. 85:158-166(2002).
CC -!- FUNCTION: Catalyzes auto- and hetero-ADP ribosylation and produces
CC short oligomers by elongating the ADP-ribose chain (up to 6-mer). Binds
CC DNA non-specifically but with high affinity. Forms very stable
CC complexes with circular DNA wherein the circular DNA confers
CC thermostability compared to linear DNA. {ECO:0000269|PubMed:11891858,
CC ECO:0000269|PubMed:11891859, ECO:0000269|PubMed:8549833,
CC ECO:0000269|PubMed:9761745}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-
CC ribosyl)n+1-acceptor + H(+).; EC=2.4.2.30;
CC Evidence={ECO:0000269|PubMed:9761745};
CC -!- ACTIVITY REGULATION: Activity increases up to 5-6 times with Mg(2+) at
CC 50 uM or higher ion concentration. 3-aminobenzamide (3-ABA) inhibits
CC the activity by up to half and nicotinamide to a lesser extent. Zn(2+)
CC inhibits the activity to half-maximal rate but at 500 uM concentration
CC of the ion. {ECO:0000269|PubMed:11040421}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=154 uM for NAD(+) {ECO:0000269|PubMed:9761745};
CC pH dependence:
CC Optimum pH is 6.5-10. {ECO:0000269|PubMed:9761745};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius. Activity decreases at 90-
CC 100 degrees Celsius. {ECO:0000269|PubMed:9761745};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; B3EWG9; -.
DR SMR; B3EWG9; -.
DR BRENDA; 2.4.2.30; 6163.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-EC.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA-binding; Glycosyltransferase; NAD;
KW Nucleotidyltransferase; Transferase.
FT CHAIN 1..>231
FT /note="NAD(+) ADP-ribosyltransferase"
FT /id="PRO_0000416971"
FT NON_CONS 46..47
FT /evidence="ECO:0000303|PubMed:19007307"
FT NON_CONS 81..82
FT /evidence="ECO:0000303|PubMed:19007307"
FT NON_CONS 102..103
FT /evidence="ECO:0000303|PubMed:19007307"
FT NON_CONS 129..130
FT /evidence="ECO:0000303|PubMed:19007307"
FT NON_CONS 185..186
FT /evidence="ECO:0000303|PubMed:19007307"
FT NON_CONS 215..216
FT /evidence="ECO:0000303|PubMed:19007307"
FT NON_TER 231
FT /evidence="ECO:0000303|PubMed:19007307"
SQ SEQUENCE 231 AA; 24334 MW; 58313193E9D78208 CRC64;
DINGGGATLP QKLYQTSGVL TAGFAPYIGV GSGNGKAAFL TNDYTKLTAT ELSTYATNLQ
PTWGKLIQVP SVATSVAIPF RITDWSGISG AGRTGPITVV YRITYMSPDF AASTLAGLDD
ATKGVSPAPS NVSDAIAQVL PPNDPSAPLD VTNPDDGVAG VQPYPDSGYP ILGFTNLIFS
AFFTKAFFTK HFGDTNNNDD AITANRFVPL PDNWKTELST YATNLQPTWG K
